Sirtuin functions and modulation: from chemistry to the clinic

Resveratrol improves health and survival of mice on a high-calorie diet

Baur, J. A., Pearson, K. J., Price, N. L., Jamieson, H. A., Lerin, C., Kalra, A., Prabhu, V. V., Allard, J. S., Lopez-Lluch, G., Lewis, K., et al. (2006) · Nature · doi:10.1038/nature05354 · Cited by 4,290

In silico analysis enabling informed design for genome editing in medicinal cannabis; gene families and variant characterisation

Calamita, E., Schmid, M., Kunz, M., Ndebele-Murisa, M. R., Magadza, C. H. D., Nyambe, I., & Wehrli, B. (2019) · Figshare · doi:10.26181/6153922fe919c · Cited by 4,239

Small molecule activators of sirtuins extend Saccharomyces cerevisiae lifespan

Howitz, K. T., Bitterman, K. J., Cohen, H. Y., Lamming, D. W., Lavu, S., Wood, J. G., Zipkin, R. E., Chung, P., Kisielewski, A., Zhang, L.-L., et al. (2003) · Nature · doi:10.1038/nature01960 · Cited by 3,796

hSIR2SIRT1 Functions as an NAD-Dependent p53 Deacetylase

Vaziri, H., Dessain, S. K., Eaton, E. N., Imai, S., Frye, R. A., Pandita, T. K., Guarente, L., & Weinberg, R. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00527-x · Cited by 2,690

Negative Control of p53 by Sir2α Promotes Cell Survival under Stress

Luo, J., Nikolaev, A. Y., Imai, S.-I., Chen, D., Su, F., Shiloh, A., Guarente, L., & Gu, W. (2001) · Cell · doi:10.1016/s0092-8674(01)00524-4 · Cited by 2,081

Calorie restriction promotes mammalian cell survival by inducing the SIRT1 deacetylase

Cohen, H. Y., Miller, C., Bitterman, K. J., Wall, N. R., Hekking, B., Kessler, B., Howitz, K. T., Gorospe, M., de Cabo, R., & Sinclair, D. A. (2004) · Science · doi:10.1126/science.1099196 · Cited by 1,924

Sirtuin activators mimic caloric restriction and delay ageing in metazoans

Wood, J. G., Rogina, B., Lavu, S., Howitz, K., Helfand, S. L., Tatar, M., & Sinclair, D. (2004) · Nature · doi:10.1038/nature02789 · Cited by 1,868

Small molecule activators of SIRT1 as therapeutics for the treatment of type 2 diabetes

Milne, J. C., Lambert, P. D., Schenk, S., Carney, D. P., Smith, J. J., Gagne, D. J., Jin, L., Boss, O., Perni, R. B., Vu, C. B., et al. (2007) · Nature · doi:10.1038/nature06261 · Cited by 1,707 · cited 1×

Sirt5 Is a NAD-Dependent Protein Lysine Demalonylase and Desuccinylase

Du, J., Zhou, Y., Su, X., Yu, J. J., Khan, S., Jiang, H., Kim, J., Woo, J., Kim, J. H., Choi, B. H., et al. (2011) · Science · doi:10.1126/science.1207861 · Cited by 1,429

The sirtuin family in health and disease

Wu, Q., Zhang, T., Chen, H., Yu, X., Lv, J.-L., Liu, Y., Liu, Y., Zheng, G., Zhao, J.-Q., Wei, Y., et al. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01257-8 · Cited by 928

Slowing ageing by design: the rise of NAD+ and sirtuin-activating compounds

Bonkowski, M. S., & Sinclair, D. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.93 · Cited by 834

Metabolic Flexibility as an Adaptation to Energy Resources and Requirements in Health and Disease

Smith, R. L., Soeters, M. R., Wüst, R. C. I., & Houtkooper, R. H. (2018) · Endocrine Reviews · doi:10.1210/er.2017-00211 · Cited by 787

Molecular Dynamics Simulations in Drug Discovery and Pharmaceutical Development

Salo‐Ahen, O. M. H., Alanko, I., Bhadane, R. N., Bonvin, A. M. J. J., Honorato, R. V., Hossain, S., Juffer, A. H., Kabedev, A., Lahtela-Kakkonen, M. K., Larsen, A. S., et al. (2020) · Processes · doi:10.3390/pr9010071 · Cited by 732

The Roles of Histone Deacetylases and Their Inhibitors in Cancer Therapy

Guo, L., Tian, Y., & Zhu, W. (2020) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.576946 · Cited by 364

The Beneficial Roles of SIRT1 in Neuroinflammation-Related Diseases

Jiao, F., & Gong, Z. (2020) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2020/6782872 · Cited by 294

SIRT6: Novel Mechanisms and Links to Aging and Disease

Tasselli, L., Zheng, W., & Chua, K. F. (2016) · Trends in Endocrinology and Metabolism · doi:10.1016/j.tem.2016.10.002 · Cited by 274

Sirtuins and Their Roles in Brain Aging and Neurodegenerative Disorders

Jęśko, H. M., Wencel, P. L., Strosznajder, R. P., & Strosznajder, J. B. (2016) · Neurochemical Research · doi:10.1007/s11064-016-2110-y · Cited by 264

Aging, oxidative stress and degenerative diseases: mechanisms, complications and emerging therapeutic strategies

Chaudhary, M. R., Chaudhary, S., Sharma, Y., Singh, T. A., Mishra, A. K., Sharma, S. G., & Mehdi, M. M. (2023) · Biogerontology · doi:10.1007/s10522-023-10050-1 · Cited by 218

SIRT1 and SIRT2 Activity Control in Neurodegenerative Diseases

Manjula, R., Anuja, K., & Alcain, F. J. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.585821 · Cited by 197

Dual Tumor Suppressor and Tumor Promoter Action of Sirtuins in Determining Malignant Phenotype

Carafa, V., Altucci, L., & Nebbioso, A. (2019) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.00038 · Cited by 186

Premature ovarian insufficiency: a review on the role of oxidative stress and the application of antioxidants

Shi, Y., Zhu, X.-T., Su-na, Z., Ma, Y., Han, Y., Yue, J., & Zhang, Y. (2023) · Frontiers in Endocrinology · doi:10.3389/fendo.2023.1172481 · Cited by 179

The role of SIRT1 in diabetic cardiomyopathy

Karbasforooshan, H., & Karimi, G. (2017) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2017.03.056 · Cited by 155

Possible Adverse Effects of High-Dose Nicotinamide: Mechanisms and Safety Assessment

Hwang, E., & Song, S. (2020) · Biomolecules · doi:10.3390/biom10050687 · Cited by 144

Sirtuin 6 protects the brain from cerebral ischemia/reperfusion injury through NRF2 activation

Zhang, W., Wei, R., Zhang, L., Tan, Y., & Qian, C. (2017) · Neuroscience · doi:10.1016/j.neuroscience.2017.09.035 · Cited by 135

How to reprogram microglia toward beneficial functions

Fumagalli, M., Lombardi, M., Gressèns, P., & Verderio, C. (2018) · Glia · doi:10.1002/glia.23484 · Cited by 134

The Interplay between Intracellular Iron Homeostasis and Neuroinflammation in Neurodegenerative Diseases

Lee, J., & Hyun, D. (2023) · Antioxidants · doi:10.3390/antiox12040918 · Cited by 142

Sirtuins and nonalcoholic fatty liver disease

Nassir, F., & Ibdah, J. A. (2016) · World Journal of Gastroenterology · doi:10.3748/wjg.v22.i46.10084 · Cited by 128

Tetrahydrocurcumin Ameliorates Diabetic Cardiomyopathy by Attenuating High Glucose-Induced Oxidative Stress and Fibrosis via Activating the SIRT1 Pathway

Li, K., Zhai, M., Jiang, L., Song, F., Zhang, B., Li, J., Li, H., Li, B., Xia, L., Xu, L. L., et al. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/6746907 · Cited by 123

Naringenin improves mitochondrial function and reduces cardiac damage following ischemia-reperfusion injury: the role of the AMPK-SIRT3 signaling pathway

Yu, L., Dong, X., Xue, X., Zhang, J., Li, Z., Wu, H., Yang, Z., Yang, Y., & Wang, H. (2019) · Food & Function · doi:10.1039/c9fo00001a · Cited by 121

Development of 1,2,4-Oxadiazoles as Potent and Selective Inhibitors of the Human Deacetylase Sirtuin 2: Structure–Activity Relationship, X-ray Crystal Structure, and Anticancer Activity

Moniot, S., Forgione, M., Lucidi, A., Hailu, G. S., Nebbioso, A., Carafa, V., Baratta, F., Altucci, L., Giacchè, N., Passeri, D., et al. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01609 · Cited by 110

Norisoboldine, a natural AhR agonist, promotes Treg differentiation and attenuates colitis via targeting glycolysis and subsequent NAD+/SIRT1/SUV39H1/H3K9me3 signaling pathway

Lv, Q., Wang, K., Qiao, S., Yang, L., Xin, Y., Dai, Y., & Wei, Z. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0297-3 · Cited by 113

Alpha-Secretase ADAM10 Regulation: Insights into Alzheimer’s Disease Treatment

Peron, R., Vatanabe, I. P., Manzine, P. R., Camins, A., & Cominetti, M. R. (2018) · Pharmaceuticals · doi:10.3390/ph11010012 · Cited by 117

DNA-Encoded Dynamic Chemical Library and Its Applications in Ligand Discovery

Zhou, Y., Li, C., Peng, J., Xie, L., Meng, L. H., Li, Q., Zhang, J., Li, X., Li, X., Huang, X., et al. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b09277 · Cited by 110

Epigenetic regulation in fibrosis progress

Xue, T., Qiu, X., Liu, H., Gan, C., Tan, Z., Xie, Y., Wang, D., & Ye, T. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105910 · Cited by 112

Lysine Deacetylase Inhibitors in Parasites: Past, Present, and Future Perspectives

Hailu, G. S., Robaa, D., Forgione, M., Sippl, W., Rotili, D., & Mai, A. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b01595 · Cited by 110

Natural Phytochemicals as SIRT Activators—Focus on Potential Biochemical Mechanisms

Wiciński, M., Erdmann, J., Nowacka, A., Kuźmiński, O., Michalak, K., Janowski, K., Ohla, J., Biernaciak, A., Szambelan, M., & Zabrzyński, J. (2023) · Nutrients · doi:10.3390/nu15163578 · Cited by 117

Microglia-Mediated Neurodegeneration in Perinatal Brain Injuries

Fleiss, B., Steenwinckel, J. V., Bokobza, C., Shearer, I. K., Ross-Munro, E., & Gressèns, P. (2021) · Biomolecules · doi:10.3390/biom11010099 · Cited by 110

SIRT1/SREBPs-mediated regulation of lipid metabolism

Shen, S., Shen, M., Kuang, L., Yang, K., Wu, S., Liu, X., Wang, Y., & Wang, Y. (2023) · Pharmacological Research · doi:10.1016/j.phrs.2023.107037 · Cited by 98

Targeting sirtuins for cancer therapy: epigenetics modifications and beyond

Shen, H., Qi, X., Hu, Y., Wang, Y., Zhang, J., Liu, Z., & Qin, Z. (2024) · Theranostics · doi:10.7150/thno.100667 · Cited by 95

Sirtuins as Important Factors in Pathological States and the Role of Their Molecular Activity Modulators

Kratz, E. M., Sołkiewicz, K., Kubis-Kubiak, A., & Piwowar, A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22020630 · Cited by 97

Histone deacetylase inhibitors for cancer therapy: An evolutionarily ancient resistance response may explain their limited success

Halsall, J. A., & Turner, B. M. (2016) · BioEssays · doi:10.1002/bies.201600070 · Cited by 87

Recent advances in the therapeutic applications of selenium nanoparticles

Ansari, J. A., Malik, J. A., Ahmed, S., Manzoor, M., Ahemad, N., & Anwar, S. (2024) · Molecular Biology Reports · doi:10.1007/s11033-024-09598-z · Cited by 85

Sirtuin 1 and Alzheimer's disease: An up-to-date review

Rizzi, L., & Roriz‐Cruz, M. (2018) · Neuropeptides · doi:10.1016/j.npep.2018.07.001 · Cited by 84

Regulation of histone deacetylase activities and functions by phosphorylation and its physiological relevance

Bahl, S., & Seto, E. (2021) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03599-4 · Cited by 82

SIRT5 promotes cell proliferation and invasion in hepatocellular carcinoma by targeting E2F1

Chang, L., Liang, X., Liu, Y., Liu, R., Wu, Z., & Jian, Z. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7875 · Cited by 81

Subcellular compartmentalization of NAD+ and its role in cancer: A sereNADe of metabolic melodies

Zhu, Y., Liu, J., Park, J., Rai, P., & Zhai, R. G. (2019) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2019.04.002 · Cited by 82

SIRT3 a Major Player in Attenuation of Hepatic Ischemia‐Reperfusion Injury by Reducing ROS via Its Downstream Mediators: SOD2, CYP‐D, and HIF‐1α

Katwal, G., Baral, D., Fan, X., He, W., Zhang, X., Li, L., Xiong, Y., Ye, Q., & Wang, Y. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/2976957 · Cited by 78

Trending topics of SIRT1 in tumorigenicity

Garcia‐Peterson, L. M., & Li, X. (2021) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2021.129952 · Cited by 77

Sirtuin Acetylation and Deacetylation: a Complex Paradigm in Neurodegenerative Disease

Khan, H., Tiwari, P., Kaur, A., & Singh, T. G. (2021) · Molecular Neurobiology · doi:10.1007/s12035-021-02387-w · Cited by 75

Suppression of SIRT1 in Diabetic Conditions Induces Osteogenic Differentiation of Human Vascular Smooth Muscle Cells via RUNX2 Signalling

Bartoli‐Leonard, F., Wilkinson, F. L., Schiro, A., Serracino‐Inglott, F., Alexander, M. Y., & Weston, R. (2019) · Scientific Reports · doi:10.1038/s41598-018-37027-2 · Cited by 76

Targeting a cryptic allosteric site of SIRT6 with small-molecule inhibitors that inhibit the migration of pancreatic cancer cells

Zhang, Q., Chen, Y., Ni, D., Huang, Z., Wei, J., Li, F., Su, J., Wei, Y., Ning, S., Yang, X., et al. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.06.015 · Cited by 74

Microplastics Exacerbate Cadmium-Induced Kidney Injury by Enhancing Oxidative Stress, Autophagy, Apoptosis, and Fibrosis

Zou, H., Chen, Y., Qu, H., Sun, J. G., Wang, T., Ma, Y., Yuan, Y., Bian, J., & Liu, Z. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214411 · Cited by 78

Energy metabolism disorders and potential therapeutic drugs in heart failure

He, Y., Huang, W., Zhang, C., Chen, L., Xu, R., Li, N., Wang, F., Han, L., Yang, M., & Zhang, D. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.007 · Cited by 74

Phloretin protects against cardiac damage and remodeling via restoring SIRT1 and anti-inflammatory effects in the streptozotocin-induced diabetic mouse model

Yin, Y., Jiang, C. S., Zhang, M., Jin, J., Ge, S., & Wang, X. (2019) · Aging · doi:10.18632/aging.101954 · Cited by 74

Diverse therapeutic efficacies and more diverse mechanisms of nicotinamide

Song, S. B., Park, J., Chung, G. J., Lee, I. H., & Hwang, E. S. (2019) · Metabolomics · doi:10.1007/s11306-019-1604-4 · Cited by 73

Metabolic requirements of the nephron

Cargill, K. R., & Sims‐Lucas, S. (2018) · Pediatric Nephrology · doi:10.1007/s00467-018-4157-2 · Cited by 71

SIRT1 and Autophagy: Implications in Endocrine Disorders

Kim, J. Y., Mondaca‐Ruff, D., Singh, S., & Wang, Y. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.930919 · Cited by 76

Extranuclear Sirtuins and Metabolic Stress

Elkhwanky, M., & Hakkola, J. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7270 · Cited by 67

Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5

Fiorentino, F., Castiello, C., Mai, A., & Rotili, D. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c00687 · Cited by 70

Histone Deacetylases and Their Inhibitors in Cancer Epigenetics

Hassell, K. N. (2019) · Diseases · doi:10.3390/diseases7040057 · Cited by 68

Groundbreaking Anticancer Activity of Highly Diversified Oxadiazole Scaffolds

Benassi, A., Doria, F., & Pirota, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21228692 · Cited by 66

Accelerated Vascular Aging in Chronic Kidney Disease: The Potential for Novel Therapies

Hobson, S., Arefin, S., Witasp, A., Hernandez, L. N., Kublickiene, K. R., Shiels, P. G., & Stenvinkel, P. (2023) · Circulation Research · doi:10.1161/circresaha.122.321751 · Cited by 64

The Role of Histone Protein Acetylation in Regulating Endothelial Function

Fang, Z. H., Wang, X., Sun, X., Hu, W., & Miao, Q. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.672447 · Cited by 66

Sirtuins as endogenous regulators of lung fibrosis: A current perspective

Mazumder, S., Barman, M., Bandyopadhyay, U., & Bindu, S. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.118201 · Cited by 61

Therapeutic effects of histone deacetylase inhibitors on heart disease

Chun, P. (2020) · Archives of Pharmacal Research · doi:10.1007/s12272-020-01297-0 · Cited by 61

SIRT3 Activation a Promise in Drug Development? New Insights into SIRT3 Biology and Its Implications on the Drug Discovery Process

Lambona, C., Zwergel, C., Valente, S., & Mai, A. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c01979 · Cited by 66

Sirtuin modulators: where are we now? A review of patents from 2015 to 2019

Mautone, N., Zwergel, C., Mai, A., & Rotili, D. (2020) · Expert Opinion on Therapeutic Patents · doi:10.1080/13543776.2020.1749264 · Cited by 57

Histone H4 lysine 16 acetylation controls central carbon metabolism and diet-induced obesity in mice

Rodrigues, C. P., Chatterjee, A., Wiese, M., Stehlé, T., Szymanski, W. G., Shvedunova, M., & Akhtar, A. (2021) · Nature Communications · doi:10.1038/s41467-021-26277-w · Cited by 58

Sirtuin Modulators: Past, Present, and Future Perspectives

Fiorentino, F., Mautone, N., Menna, M., D’Acunzo, F., Mai, A., & Rotili, D. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2022-0031 · Cited by 57

Salivary Biomarkers for Alzheimer’s Disease: A Systematic Review with Meta-Analysis

Nijakowski, K., Owecki, W., Jankowski, J., & Surdacka, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25021168 · Cited by 65

Role of SIRT1 and Progesterone Resistance in Normal and Abnormal Endometrium

Kim, T. H., Young, S. L., Sasaki, T., Deaton, J. L., Schammel, D. P., Palomino, W. A., Jeong, J., & Lessey, B. A. (2021) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/clinem/dgab753 · Cited by 55

Protection of the myocardium against ischemia/reperfusion injury by punicalagin through an SIRT1-NRF-2-HO-1-dependent mechanism

Yu, L., Dong, X., Xue, X., Zhang, J., Li, Z., Wu, H., Yang, Z., Yang, Y., & Wang, H. (2019) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2019.05.003 · Cited by 55

Growth factor, energy and nutrient sensing signalling pathways in metabolic ageing

Bettedi, L., & Foukas, L. C. (2017) · Biogerontology · doi:10.1007/s10522-017-9724-6 · Cited by 55

Sirtuin-4 (SIRT4), a therapeutic target with oncogenic and tumor-suppressive activity in cancer

Huang, G., & Zhu, G. (2018) · OncoTargets and Therapy · doi:10.2147/ott.s157724 · Cited by 53

RIP1–HAT1–SIRT Complex Identification and Targeting in Treatment and Prevention of Cancer

Carafa, V., Nebbioso, A., Cuomo, F., Rotili, D., Cobellis, G., Bontempo, P., Baldi, A., Spugnini, E. P., Citro, G., Chambery, A., et al. (2018) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-3081 · Cited by 51

Diabetic retinopathy, oxidative stress, and sirtuins: an in depth look in enzymatic patterns and new therapeutic horizons

Nebbioso, M., Lambìase, A., Armentano, M., Tucciarone, G., Sacchetti, M., Greco, A., & Alisi, L. (2021) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2021.04.003 · Cited by 53

Inhibition of sirtuins 1 and 2 impairs cell survival and migration and modulates the expression of P-glycoprotein and MRP3 in hepatocellular carcinoma cell lines

Ceballos, M. P., Decándido, G., Quiroga, A. D., Comanzo, C. G., Livore, V. I., Lorenzetti, F., Lambertucci, F., Chazarreta-Cifre, L., Banchio, C., Álvarez, M. D. L., et al. (2018) · Toxicology Letters · doi:10.1016/j.toxlet.2018.03.011 · Cited by 49

The Role of Sirtuin 1 (SIRT1) in Neurodegeneration

Razick, D., Akhtar, M., Wen, J., Alam, M., Dean, N., Karabala, M., Ansari, U., Ansari, Z., Tabaie, E. A., & Siddiqui, S. (2023) · Cureus · doi:10.7759/cureus.40463 · Cited by 48

Therapeutic effects of histone deacetylase inhibitors on kidney disease

Chun, P. (2017) · Archives of Pharmacal Research · doi:10.1007/s12272-017-0998-7 · Cited by 48

Human sirtuins: Structures and flexibility

Sacconnay, L., Carrupt, P., & Nurisso, A. (2016) · Journal of Structural Biology · doi:10.1016/j.jsb.2016.10.008 · Cited by 47

Bone marrow mesenchymal stem cell exosomes suppress phosphate-induced aortic calcification via SIRT6–HMGB1 deacetylation

Wei, W., Guo, X., Gu, L., Jia, J., Yang, M. G., Yuan, W., & Rong, S. (2021) · Stem Cell Research & Therapy · doi:10.1186/s13287-021-02307-8 · Cited by 47

Imidazo[1,2-b]pyridazine as privileged scaffold in medicinal chemistry: An extensive review

Garrido, A., Vera, G., Delaye, P., & Enguehard‐Gueiffier, C. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113867 · Cited by 47

Neurotrophic effects of intermittent fasting, calorie restriction and exercise: a review and annotated bibliography

Mayor, E. (2023) · Frontiers in Aging · doi:10.3389/fragi.2023.1161814 · Cited by 47

DNA hypermethylation of sirtuin 1 (SIRT1) caused by betel quid chewing—a possible predictive biomarker for malignant transformation

Islam, S., Uehara, O., Matsuoka, H., Kuramitsu, Y., Adhikari, B. R., Hiraki, D., Toraya, S., Jayawardena, A., Saito, I., Muthumala, M., et al. (2020) · Clinical Epigenetics · doi:10.1186/s13148-019-0806-y · Cited by 45

Terminal Schwann Cell Aging: Implications for Age-Associated Neuromuscular Dysfunction

Fuertes-Álvarez, S., & Izeta, A. (2021) · Aging and Disease · doi:10.14336/ad.2020.0708 · Cited by 46

Fruits: A Source of Polyphenols and Health Benefits

Calderón‐Oliver, M., & Ponce‐Alquicira, E. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-811518-3.00007-7 · Cited by 46

Cardioprotective effect of a moderate and prolonged exercise training involves sirtuin pathway

Donniacuo, M., Urbanek, K., Nebbioso, A., Sodano, L., Gallo, L., Altucci, L., & Rinaldi, B. (2019) · Life Sciences · doi:10.1016/j.lfs.2019.03.001 · Cited by 42

Epigenetic repression of Wnt receptors in AD: a role for Sirtuin2-induced H4K16ac deacetylation of Frizzled1 and Frizzled7 promoters

Palomer, E., Martín‐Flores, N., Jolly, S., Vargas, P. P., Benvegnù, S., Podpolny, M., Teo, S., Vaher, K., Saito, T., Saido, T. C., et al. (2022) · Molecular Psychiatry · doi:10.1038/s41380-022-01492-z · Cited by 42

Multiple myeloma, a quintessential malignant disease of aging: a geroscience perspective on pathogenesis and treatment

Urbán, V. S., Ceglédi, A., & Mikala, G. (2022) · GeroScience · doi:10.1007/s11357-022-00698-x · Cited by 43

Anticancer Activities of a Benzimidazole Compound Through Sirtuin Inhibition in Colorectal Cancer

Tan, Y. J., Lee, Y. T., Yeong, K. Y., Petersen, S. H., Kono, K., Tan, S. C., & Oon, C. E. (2018) · Future Medicinal Chemistry · doi:10.4155/fmc-2018-0052 · Cited by 39

Melatonin as Potential Targets for Delaying Ovarian Aging

Yang, Y., Cheung, H., Zhang, C., Wu, J., & Chan, W. (2018) · Current Drug Targets · doi:10.2174/1389450119666180828144843 · Cited by 39

Effects of (−)-epicatechin on mitochondria

Daussin, F., Heyman, E., & Burelle, Y. (2020) · Nutrition Reviews · doi:10.1093/nutrit/nuaa094 · Cited by 39

Sirtuin Modulators in Cellular and Animal Models of Human Diseases

Hong, J. Y., & Lin, H. (2021) · Frontiers in Pharmacology · doi:10.3389/fphar.2021.735044 · Cited by 40

Sirtuins in metabolism, stemness and differentiation

Correia, M., Perestrelo, T., Rodrigues, A. S., Ribeiro, M. F., Pereira, S. L., Sousa, M. I., & Ramalho‐Santos, J. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.09.008 · Cited by 40

Histone deacetylases as targets in autoimmune and autoinflammatory diseases

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